PRE3/YJL001W Literature Guide Help

Other names published for PRE3: CRL21, proteasome core particle subunit beta 1, YJL001W

PRE3 - Mutants/Phenotypes (23)

ReferenceOther Genes Addressed
Mishto M, et al.  (2012) Driving forces of proteasome-catalyzed peptide splicing in yeast and humans. Mol Cell Proteomics 11(10):1008-23
Tallec BL and Peyroche A  (2012) Using DNA damage sensitivity phenotypes to characterize mutations affecting proteasome function. Methods Mol Biol 832():363-71
Park S, et al.  (2011) Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. J Biol Chem 286(42):36652-66
Collins GA, et al.  (2010) Combined chemical and genetic approach to inhibit proteolysis by the proteasome. Yeast 27(11):965-74
Osmulski PA, et al.  (2009) A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel. Structure 17(8):1137-47
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Ganguli D, et al.  (2007) The Alternative Pathway of Glutathione Degradation Is Mediated by a Novel Protein Complex Involving Three New Genes in Saccharomyces cerevisiae. Genetics 175(3):1137-51
Hervas-Aguilar A, et al.  (2007) Evidence for the Direct Involvement of the Proteasome in the Proteolytic Processing of the Aspergillus nidulans Zinc Finger Transcription Factor PacC. J Biol Chem 282(48):34735-47
Juneau K, et al.  (2006) Introns regulate RNA and protein abundance in yeast. Genetics 174(1):511-8
Altmann K and Westermann B  (2005) Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol Biol Cell 16(11):5410-7
Ramos PC, et al.  (2004) Role of C-terminal extensions of subunits beta2 and beta7 in assembly and activity of eukaryotic proteasomes. J Biol Chem 279(14):14323-30
Podlaska A, et al.  (2003) The link between 20S proteasome activity and post-replication DNA repair in Saccharomyces cerevisiae. Mol Microbiol 49(5):1321-32
Arendt CS and Hochstrasser M  (1999) Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J 18(13):3575-85
Groll M, et al.  (1999) The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc Natl Acad Sci U S A 96(20):10976-83
Jager S, et al.  (1999) Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function. J Mol Biol 291(4):997-1013
Ditzel L, et al.  (1998) Conformational constraints for protein self-cleavage in the proteasome. J Mol Biol 279(5):1187-91
Gueckel R, et al.  (1998) Mutations in the yeast proteasome beta-type subunit Pre3 uncover position-dependent effects on proteasomal peptidase activity and in vivo function. J Biol Chem 273(31):19443-52
Arendt CS and Hochstrasser M  (1997) Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc Natl Acad Sci U S A 94(14):7156-61
Gerlinger UM, et al.  (1997) Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation. Mol Biol Cell 8(12):2487-99
Heinemeyer W, et al.  (1997) The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J Biol Chem 272(40):25200-9
Enenkel C, et al.  (1994) PRE3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity. FEBS Lett 341(2-3):193-6
McCusker JH and Haber JE  (1988) Cycloheximide-resistant temperature-sensitive lethal mutations of Saccharomyces cerevisiae. Genetics 119(2):303-15
McCusker JH and Haber JE  (1988) crl mutants of Saccharomyces cerevisiae resemble both mutants affecting general control of amino acid biosynthesis and omnipotent translational suppressor mutants. Genetics 119(2):317-27